PMID:9008164

Citation	Bycroft, M, Hubbard, TJ, Proctor, M, Freund, SM and Murzin, AG (1997) The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Cell 88:235-42
Abstract	The S1 domain, originally identified in ribosomal protein S1, is found in a large number of RNA-associated proteins. The structure of the S1 RNA-binding domain from the E. coli polynucleotide phosphorylase has been determined using NMR methods and consists of a five-stranded antiparallel beta barrel. Conserved residues on one face of the barrel and adjacent loops form the putative RNA-binding site. The structure of the S1 domain is very similar to that of cold shock protein, suggesting that they are both derived from an ancient nucleic acid-binding protein. Enhanced sequence searches reveal hitherto unidentified S1 domains in RNase E, RNase II, NusA, EMB-5, and other proteins.
Links	PubMed
Keywords	Amino Acid Sequence; Bacterial Proteins/chemistry; Binding Sites; Cold Temperature; Crystallography, X-Ray; Escherichia coli/enzymology; Eukaryotic Initiation Factor-2/metabolism; Fungal Proteins/chemistry; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Phosphorylation; Polyribonucleotide Nucleotidyltransferase/chemistry; Polyribonucleotide Nucleotidyltransferase/metabolism; Protein Conformation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Protein-Serine-Threonine Kinases/metabolism; RNA/metabolism; RNA-Binding Proteins/chemistry; RNA-Binding Proteins/metabolism; Ribosomal Proteins/chemistry; eIF-2 Kinase
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